Found 2699 results
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Xu, H., Faber, C., Uchiki, T., Racca, J., and Dealwis, C. (2006) Structures of eukaryotic ribonucleotide reductase I define gemcitabine diphosphate binding and subunit assembly. Proc Natl Acad Sci U S A. 103, 4028-33
Xu, X., Choi, S. Hee, Hu, T., Tiyanont, K., Habets, R., Groot, A. J., Vooijs, M., Aster, J. C., Chopra, iv, R., Fryer, C., and Blacklow, S. C. (2015) Insights into Autoregulation of Notch3 from Structural and Functional Studies of Its Negative Regulatory Region. Structure. 23, 1227-35
Xu, S., Uddin, M. Jashim, Banerjee, S., Duggan, K., Musee, J., Kiefer, J. R., Ghebreselasie, K., Rouzer, C. A., and Marnett, L. J. (2019) Fluorescent indomethacin-dansyl conjugates utilize the membrane-binding domain of cyclooxygenase-2 to block the opening to the active site. J Biol Chem. 10.1074/jbc.RA119.007405
Xu, G., Lo, Y. - C., Li, Q., Napolitano, G., Wu, X., Jiang, X., Dreano, M., Karin, M., and Wu, H. (2011) Crystal structure of inhibitor of κB kinase β.. Nature. 472, 325-30
Xu, K., Xu, Y., Rajashankar, K. R., Robev, D., and Nikolov, D. B. (2013) Crystal structures of Lgr4 and its complex with R-spondin1. Structure. 21, 1683-9
Xu, Y., Moseley, J. B., Sagot, I., Poy, F., Pellman, D., Goode, B. L., and Eck, M. J. (2004) Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture. Cell. 116, 711-23
Xu, Y., Tao, Y., Cheung, L. S., Fan, C., Chen, L. - Q., Xu, S., Perry, K., Frommer, W. B., and Feng, L. (2014) Structures of bacterial homologues of SWEET transporters in two distinct conformations. Nature. 515, 448-52
Xu, K., Olsen, O., Tzvetkova-Robev, D., Tessier-Lavigne, M., and Nikolov, D. B. (2015) The crystal structure of DR6 in complex with the amyloid precursor protein provides insight into death receptor activation. Genes Dev. 29, 785-90
Xu, K., Tzvetkova-Robev, D., Xu, Y., Goldgur, Y., Chan, Y. - P., Himanen, J. P., and Nikolov, D. B. (2013) Insights into Eph receptor tyrosine kinase activation from crystal structures of the EphA4 ectodomain and its complex with ephrin-A5. Proc Natl Acad Sci U S A. 110, 14634-9
Xu, S., Hermanson, D. J., Banerjee, S., Ghebreselasie, K., Clayton, G. M., R Garavito, M., and Marnett, L. J. (2014) Oxicams bind in a novel mode to the cyclooxygenase active site via a two-water-mediated H-bonding Network. J Biol Chem. 289, 6799-808
Xu, K., Chan, Y. - P., Bradel-Tretheway, B., Akyol-Ataman, Z., Zhu, Y., Dutta, S., Yan, L., Feng, Y. R., Wang, L. - F., Skiniotis, G., Lee, B., Z Zhou, H., Broder, C. C., Aguilar, H. C., and Nikolov, D. B. (2015) Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly. PLoS Pathog. 11, e1005322
Xu, Y., Robev, D., Saha, N., Wang, B., Dalva, M. B., Xu, K., Himanen, J. P., and Nikolov, D. B. (2021) The Ephb2 Receptor Uses Homotypic, Head-to-Tail Interactions within Its Ectodomain as an Autoinhibitory Control Mechanism. Int J Mol Sci. 10.3390/ijms221910473
Xu, K., Rockx, B., Xie, Y., DeBuysscher, B. L., Fusco, D. L., Zhu, Z., Chan, Y. - P., Xu, Y., Luu, T., Cer, R. Z., Feldmann, H., Mokashi, V., Dimitrov, D. S., Bishop-Lilly, K. A., Broder, C. C., and Nikolov, D. B. (2013) Crystal structure of the Hendra virus attachment G glycoprotein bound to a potent cross-reactive neutralizing human monoclonal antibody. PLoS Pathog. 9, e1003684
Xu, K., Wu, Z., Renier, N., Antipenko, A., Tzvetkova-Robev, D., Xu, Y., Minchenko, M., Nardi-Dei, V., Rajashankar, K. R., Himanen, J., Tessier-Lavigne, M., and Nikolov, D. B. (2014) Neural migration. Structures of netrin-1 bound to two receptors provide insight into its axon guidance mechanism. Science. 344, 1275-9
Xue, S., Calvin, K., and Li, H. (2006) RNA recognition and cleavage by a splicing endonuclease. Science. 312, 906-10
Yamaguchi, M., Yu, S., Qiao, R., Weissmann, F., Miller, D. J., VanderLinden, R., Brown, N. G., Frye, J. J., Peters, J. - M., and Schulman, B. A. (2015) Structure of an APC3-APC16 complex: insights into assembly of the anaphase-promoting complex/cyclosome. J Mol Biol. 427, 1748-64
Yan, X., Wang, X., Li, Y., Zhou, M., Li, Y., Song, L., Mi, W., Min, J., and Dong, C. (2021) Molecular basis for ubiquitin ligase CRL2-mediated recognition of C-degron. Nat Chem Biol. 10.1038/s41589-020-00703-4
Yan, W., Markegard, E., Dharmaiah, S., Urisman, A., Drew, M., Esposito, D., Scheffzek, K., Nissley, D. V., McCormick, F., and Simanshu, D. K. (2020) Structural Insights into the SPRED1-Neurofibromin-KRAS Complex and Disruption of SPRED1-Neurofibromin Interaction by Oncogenic EGFR. Cell Rep. 32, 107909
Yang, H., Wang, J., Jia, X., McNatt, M. W., Zang, T., Pan, B., Meng, W., Wang, H. - W., Bieniasz, P. D., and Xiong, Y. (2010) Structural insight into the mechanisms of enveloped virus tethering by tetherin. Proc Natl Acad Sci U S A. 107, 18428-32
Yang, H., Rudge, D. G., Koos, J. D., Vaidialingam, B., Yang, H. J., and Pavletich, N. P. (2013) mTOR kinase structure, mechanism and regulation. Nature. 497, 217-23
Yang, Y., Liu, X. Roger, Greenberg, Z. J., Zhou, F., He, P., Fan, L., Liu, S., Shen, G., Egawa, T., Gross, M. L., Schuettpelz, L. G., and Li, W. (2020) Open conformation of tetraspanins shapes interaction partner networks on cell membranes. EMBO J. 39, e105246
Yang, M. Hee, Tran, T. H., Hunt, B., Agnor, R., Johnson, C. W., Shui, B., Waybright, T. J., Nowak, J. A., Stephen, A. G., Simanshu, D. K., and Haigis, K. M. (2023) Allosteric Regulation of Switch-II Domain Controls KRAS Oncogenicity. Cancer Res. 83, 3176-3183
Yang, Y., Ke, N., Liu, S., and Li, W. (2017) Methods for Structural and Functional Analyses of Intramembrane Prenyltransferases in the UbiA Superfamily. Methods Enzymol. 584, 309-347
Yang, G., Fu, Y., Malakhova, M., Kurinov, I., Zhu, F., Yao, K., Li, H., Chen, H., Li, W., Lim, D. Young, Sheng, Y., Bode, A. M., Dong, Z., and Dong, Z. (2014) Caffeic acid directly targets ERK1/2 to attenuate solar UV-induced skin carcinogenesis. Cancer Prev Res (Phila). 7, 1056-66
Yang, Y., Harris, K. A., Widner, D. L., and Breaker, R. R. (2021) Structure of a bacterial OapB protein with its OLE RNA target gives insights into the architecture of the OLE ribonucleoprotein complex. Proc Natl Acad Sci U S A. 10.1073/pnas.2020393118